The specificity and localization of monoclonal antibodies against sperm-specific lactate dehydrogenase C4

Wang, S.X; Luo, An-Ming; Liang, Zhiting; Song, Jianming; Wang, H.A; Chen, Y.X

doi:10.1016/0165-0378(89)90119-8

Cited by 6 publications

(8 citation statements)

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“…By immunofluorescence with specific antibody we localized this isozyme to the principle piece of the sperm tail, similar to compartmentalization reported for other glycolytic enzymes. We could not confirm the result of Wang et al (1990) that mouse sperm LDH-C 4 localized to the mid-piece of the sperm flagellum. The finding by Burgos et al (1995) that LDH-C 4 is in mouse sperm mitochondria is also not in agreement with our data.…”

confidence: 52%

“…Subsequently, Blanco et al (1976) re-examined their assay procedures and found that in mouse testis extracts about 60 % of total LDH-C 4 was in the "soluble phase", 20 % of LDH-C 4 was in "sperm-specific mitochondria" and the rest was not identified. Wang et al (1990) reported LDH-C 4 localized to the post-acrosome area and midpiece of human sperm, but only to the mid-piece of mouse sperm. Burgos et al (1995) examined LDH-C 4 distribution in mouse sperm by electron microscopy and observed localization to the cytoplasm of the mid-piece and principal piece, as well as to sperm mitochondria.…”

Section: Effect Of Glycolytic Inhibitors On Sperm Protein Tyrosine Phmentioning

confidence: 99%

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Inhibition of lactate dehydrogenase C4 (LDH-C4) blocks capacitation of mouse sperm in vitro

Duan

Goldberg

2003

Cytogenet Genome Res

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Lactate dehydrogenase C₄ (LDH-C₄) is a tissue-specific enzyme in the mammalian testis and the only lactate dehydrogenase isozyme of sperm. Inhibitors of LDH activity were used to determine whether this enzyme plays a role in sperm capacitation, the acrosome reaction and/or fertilization. Oxamate or its derivative was used to inhibit sperm LDH activity in a medium promoting capacitation. Complete inhibition of LDH activity blocked capacitation. This effect could be reversed partially by the addition of dbcAMP or pentoxifylline to the culture medium. Western blotting showed that oxamate and N-isopropyl oxamate inhibited the tyrosine phosphorylation of proteins during the sperm capacitation process. Presumably, glycolysis is the primary energy pathway for sperm metabolism. The oxidation of reduced NAD with the conversion of pyruvate to lactate by LDH provides ATP necessary for protein kinase A (PKA) activity. Our data indicate that LDH-C₄ plays an important metabolic role in sperm capacitation.

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confidence: 52%

Section: Effect Of Glycolytic Inhibitors On Sperm Protein Tyrosine Phmentioning

confidence: 99%

Inhibition of lactate dehydrogenase C4 (LDH-C4) blocks capacitation of mouse sperm in vitro

Duan

Goldberg

2003

Cytogenet Genome Res

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“…The postpubertal testis and sperm contain another LDH isoenzyme commonly named LDH-X or LDH-C4 (Blanco & Zinkham, 1963;Zinkham et af., 1964) which is specific for post-meiotic germ cells and sperm (Hintz & Goldberg, 1977;Meinstrich et al, 1977;BellvC et al, 1989). Recently, LDH-X has been localized to the post-acrosome region, neck and midpiece of human sperm by immunofluorescence assay (Wang et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

LDH and LDH‐X activity in sperm from normospermic and oligozoospermic men

et al. 1991

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Total lactate dehydrogenase (LDH) activity was measured in washed sperm from 74 oligozoospermic patients and 148 normospermic men. In the same samples, an additional iso-enzyme specific for germ cells, LDH-X was also measured. Both enzymatic activities were significantly higher in sperm from oligozoospermic patients than in those from normospermic men (P less than 0.001). In oligozoospermic patients, sperm LDH and LDH-X activities were related inversely to sperm concentration (r = -0.61 and r = -0.53, respectively). In normospermic men, this inverse relationship was less evident (r = -0.28 and r = -0.25, respectively). After separation of sperm on a discontinuous gradient of Percoll, LDH and LDH-X activities were increased in the non-migrated-sperm fractions and reduced in the migrated-sperm fractions in both groups of subjects when compared to the initial semen specimens. In addition, migrated sperm from oligozoospermic and normospermic men did not differ in their LDH and LDH-X activities. Although the possible contribution of immature germ-cells to these findings remains to be defined, the data suggest clearly that high levels of intracellular LDH and LDH-X are a biochemical feature of sperm from oligozoospermic subjects.

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“…4). In each case, lactate formation could occur in cytosol or mitochondria, as sperm-specific lactate dehydrogenase has been found in these compartments [64][65][66][67]. Lactate and NADH production also could occur in separate cellular locations, since reducing equivalents can be transferred between the cytosol and mitochondria by the malate-aspartate shuttle (present in spermatozoa of several species [68][69][70]).…”

Section: Discussionmentioning

confidence: 99%

Evidence for Compromised Metabolic Function and Limited Glucose Uptake in Spermatozoa from the Teratospermic Domestic Cat (Felis catus) and Cheetah (Acinonyx jubatus)1

Terrell

Wildt

Anthony

et al. 2010

Biology of Reproduction

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Cheetahs and certain other felids consistently ejaculate high proportions (!60%) of malformed spermatozoa, a condition known as teratospermia, which is prevalent in humans. Even seemingly normal spermatozoa from domestic cat teratospermic ejaculates have reduced fertilizing capacity. To understand the role of sperm metabolism in this phenomenon, we conducted a comparative study in the normospermic domestic cat versus the teratospermic cat and cheetah with the general hypothesis that sperm metabolic function is impaired in males producing predominantly pleiomorphic spermatozoa. Washed ejaculates were incubated in chemically defined medium containing glucose and pyruvate. Uptake of glucose and pyruvate and production of lactate were assessed using enzyme-linked fluorescence assays. Spermatozoa from domestic cats and cheetahs exhibited similar metabolic profiles, with minimal glucose metabolism and approximately equimolar rates of pyruvate uptake and lactate production. Compared to normospermic counterparts, pyruvate and lactate metabolism were reduced in teratospermic cat and cheetah ejaculates, even when controlling for sperm motility. Rates of pyruvate and lactate (but not glucose) metabolism were correlated positively with sperm motility, acrosomal integrity, and normal morphology. Collectively, our findings reveal that pyruvate uptake and lactate production are reliable, quantitative indicators of sperm quality in these two felid species and that metabolic function is impaired in teratospermic ejaculates. Furthermore, patterns of substrate utilization are conserved between these species, including the unexpected lack of exogenous glucose metabolism. Because glycolysis is required to support sperm motility and capacitation in certain other mammals (including dogs), the activity of this pathway in felid spermatozoa is a target for future investigation.

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The specificity and localization of monoclonal antibodies against sperm-specific lactate dehydrogenase C4

Cited by 6 publications

References 0 publications

Inhibition of lactate dehydrogenase C<sub>4</sub> (LDH-C<sub>4</sub>) blocks capacitation of mouse sperm in vitro

Inhibition of lactate dehydrogenase C<sub>4</sub> (LDH-C<sub>4</sub>) blocks capacitation of mouse sperm in vitro

LDH and LDH‐X activity in sperm from normospermic and oligozoospermic men

Evidence for Compromised Metabolic Function and Limited Glucose Uptake in Spermatozoa from the Teratospermic Domestic Cat (Felis catus) and Cheetah (Acinonyx jubatus)1

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